TAILIEUCHUNG - Báo cáo khoa học: Gradual phosphorylation regulates PC4 coactivator function

The unstructured N-terminal domain of the transcriptional cofactor PC4 contains multiple phosphorylation sites that regulate activity. The phos-phorylation status differentially influences the various biochemical func-tions performed by the structured core of PC4. Binding to ssDNA is slightly enhanced by phosphorylation of one serine residue, which is not augmented by further phosphorylation. | iFEBS Journal Gradual phosphorylation regulates PC4 coactivator function Hendrik R. A. Jonker1 Rainer W. Wechselberger1 Martijn Pinkse2 Robert Kaptein1 and Gert E. Folkers1 1 Department of NMR Spectroscopy Bijvoet Center for Biomolecular Research Utrecht University the Netherlands 2 Department of Biomolecular Mass Spectrometry Utrecht University the Netherlands Keywords casein kinase II PC4 phosphorylation transcription RNA polymerase II Correspondence G. E. Folkers Bijvoet Center for Biomolecular Research Section NMR spectroscopy Utrecht University Padualaan 8 3584 CH Utrecht the Netherlands Fax 31 30 253 7623 Tel 31 30 253 9930 E-mail H. R. A. Jonker . Goethe University -Center for Biomolecular NMR Institute for Organic Chemistry and ChemicalBiology Marie Curie Strasse 11 N160 312 D-60439 Frankfurt am Main Germany Fax 49 69 798 29515 Tel 49 69 798 29137 E-mail henry@ Received 14 December 2005 revised 30 January 2006 accepted 3 February 2006 doi The unstructured N-terminal domain of the transcriptional cofactor PC4 contains multiple phosphorylation sites that regulate activity. The phosphorylation status differentially influences the various biochemical functions performed by the structured core of PC4. Binding to ssDNA is slightly enhanced by phosphorylation of one serine residue which is not augmented by further phosphorylation. The presence of at least two phosphoserines decreases DNA-unwinding activity and abrogates binding to the transcriptional activator VP16. Phosphorylation gradually decreases the binding affinity for dsDNA. These phosphorylation-dependent changes in PC4 activities correlate with the sequential functions PC4 fulfils throughout the transcription cycle. MS and NMR revealed that up to eight serines are progressively phosphorylated towards the N-terminus resulting in gradual environmental changes in the C-terminal direction of the following lysine-rich region. Also within the .

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